ELAV1_HUMAN
ID ELAV1_HUMAN Reviewed; 326 AA.
AC Q15717; B4DVB8; Q53XN6; Q9BTT1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=ELAV-like protein 1;
DE AltName: Full=Hu-antigen R;
DE Short=HuR {ECO:0000303|PubMed:8626503};
GN Name=ELAVL1; Synonyms=HUR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, RNA-BINDING, AND TISSUE
RP SPECIFICITY.
RX PubMed=8626503; DOI=10.1074/jbc.271.14.8144;
RA Ma W.-J., Cheng S., Campbell C., Wright A., Furneaux H.M.;
RT "Cloning and characterization of HuR, a ubiquitously expressed Elav-like
RT protein.";
RL J. Biol. Chem. 271:8144-8151(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH ANP32A.
RX PubMed=11729309; DOI=10.1126/science.1064693;
RA Gallouzi I.-E., Steitz J.A.;
RT "Delineation of mRNA export pathways by the use of cell-permeable
RT peptides.";
RL Science 294:1895-1901(2001).
RN [8]
RP METHYLATION AT ARG-217.
RX PubMed=12237300; DOI=10.1074/jbc.m206187200;
RA Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W.,
RA Stallcup M.R., Laird-Offringa I.A.;
RT "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing
RT protein, by CARM1. Coactivator-associated arginine methyltransferase.";
RL J. Biol. Chem. 277:44623-44630(2002).
RN [9]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY
RP MAPKAPK2.
RX PubMed=14517288; DOI=10.1128/mcb.23.20.7177-7188.2003;
RA Tran H., Maurer F., Nagamine Y.;
RT "Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked
RT to its cytoplasmic accumulation induced by activated mitogen-activated
RT protein kinase-activated protein kinase 2.";
RL Mol. Cell. Biol. 23:7177-7188(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP INTERACTION WITH DHX36 AND ILF3, AND RNA-BINDING.
RX PubMed=14731398; DOI=10.1016/s1097-2765(03)00481-7;
RA Tran H., Schilling M., Wirbelauer C., Hess D., Nagamine Y.;
RT "Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH
RT protein RHAU.";
RL Mol. Cell 13:101-111(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein
RT complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17632515; DOI=10.1038/nchembio.2007.14;
RA Meisner N.C., Hintersteiner M., Mueller K., Bauer R., Seifert J.M.,
RA Naegeli H.U., Ottl J., Oberer L., Guenat C., Moss S., Harrer N.,
RA Woisetschlaeger M., Buehler C., Uhl V., Auer M.;
RT "Identification and mechanistic characterization of low-molecular-weight
RT inhibitors for HuR.";
RL Nat. Chem. Biol. 3:508-515(2007).
RN [16]
RP INTERACTION WITH PLEKHN1.
RX PubMed=18191643; DOI=10.1016/j.bbamcr.2007.12.009;
RA Sano E., Shono S., Tashiro K., Konishi H., Yamauchi E., Taniguchi H.;
RT "Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP
RT functions as mitochondrial RNA granule.";
RL Biochim. Biophys. Acta 1783:1036-1047(2008).
RN [17]
RP INTERACTION WITH HNRNPL.
RX PubMed=18161049; DOI=10.1002/hep.22036;
RA Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M.,
RA Kaibori M., Kamiyama Y., Ito S., Okumura T.;
RT "Natural antisense transcript stabilizes inducible nitric oxide synthase
RT messenger RNA in rat hepatocytes.";
RL Hepatology 47:686-697(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [19]
RP RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-158;
RP SER-221 AND SER-318, AND MUTAGENESIS OF SER-158; SER-221 AND SER-318.
RX PubMed=18285462; DOI=10.1128/mcb.01530-07;
RA Doller A., Akool E.-S., Huwiler A., Mueller R., Radeke H.H.,
RA Pfeilschifter J., Eberhardt W.;
RT "Posttranslational modification of the AU-rich element binding protein HuR
RT by protein kinase Cdelta elicits angiotensin II-induced stabilization and
RT nuclear export of cyclooxygenase 2 mRNA.";
RL Mol. Cell. Biol. 28:2608-2625(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP RNA-BINDING.
RX PubMed=19561594; DOI=10.1038/nbt.1550;
RA Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S.,
RA Blencowe B.J., Morris Q., Hughes T.R.;
RT "Rapid and systematic analysis of the RNA recognition specificities of RNA-
RT binding proteins.";
RL Nat. Biotechnol. 27:667-670(2009).
RN [22]
RP FUNCTION, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND SER-202, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
RX PubMed=23640942; DOI=10.1515/hsz-2013-0111;
RA Wachter K., Kohn M., Stohr N., Huttelmaier S.;
RT "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding
RT proteins) is modulated by distinct RNA-binding domains.";
RL Biol. Chem. 394:1077-1090(2013).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-197 AND SER-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-217, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [31]
RP INTERACTION WITH PLEKHN1.
RX PubMed=27616329; DOI=10.1016/j.bbalip.2016.09.006;
RA Nishino T., Matsunaga R., Jikihara H., Uchida M., Maeda A., Qi G., Abe T.,
RA Kiyonari H., Tashiro S., Inagaki-Ohara K., Shimamoto F., Konishi H.;
RT "Antagonizing effect of CLPABP on the function of HuR as a regulator of
RT ARE-containing leptin mRNA stability and the effect of its depletion on
RT obesity in old male mouse.";
RL Biochim. Biophys. Acta 1861:1816-1827(2016).
RN [32]
RP INTERACTION WITH SHFL.
RX PubMed=27974568; DOI=10.1128/jvi.01606-16;
RA Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K.,
RA Zoon K.C.;
RT "IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity
RT against Dengue Virus, Interacts with MOV10.";
RL J. Virol. 91:0-0(2017).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP FUNCTION.
RX PubMed=29180010; DOI=10.1016/j.bbrc.2017.11.112;
RA Maeda A., Uchida M., Nishikawa S., Nishino T., Konishi H.;
RT "Role of N-myristoylation in stability and subcellular localization of the
RT CLPABP protein.";
RL Biochem. Biophys. Res. Commun. 495:1249-1256(2018).
RN [35]
RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3, AND SUBCELLULAR LOCATION.
RX PubMed=29476152; DOI=10.1038/s41556-018-0045-z;
RA Huang H., Weng H., Sun W., Qin X., Shi H., Wu H., Zhao B.S., Mesquita A.,
RA Liu C., Yuan C.L., Hu Y.C., Huettelmaier S., Skibbe J.R., Su R., Deng X.,
RA Dong L., Sun M., Li C., Nachtergaele S., Wang Y., Hu C., Ferchen K.,
RA Greis K.D., Jiang X., Wei M., Qu L., Guan J.L., He C., Yang J., Chen J.;
RT "Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA
RT stability and translation.";
RL Nat. Cell Biol. 20:285-295(2018).
RN [36]
RP FUNCTION, AND INTERACTION WITH YBX1.
RX PubMed=31358969; DOI=10.1038/s41556-019-0361-y;
RA Chen X., Li A., Sun B.F., Yang Y., Han Y.N., Yuan X., Chen R.X., Wei W.S.,
RA Liu Y., Gao C.C., Chen Y.S., Zhang M., Ma X.D., Liu Z.W., Luo J.H., Lyu C.,
RA Wang H.L., Ma J., Zhao Y.L., Zhou F.J., Huang Y., Xie D., Yang Y.G.;
RT "5-methylcytosine promotes pathogenesis of bladder cancer through
RT stabilizing mRNAs.";
RL Nat. Cell Biol. 21:978-990(2019).
RN [37]
RP FUNCTION, AND INTERACTION WITH IGF2BP1.
RX PubMed=32245947; DOI=10.1038/s41467-020-15403-9;
RA Zhu S., Wang J.Z., Chen D., He Y.T., Meng N., Chen M., Lu R.X., Chen X.H.,
RA Zhang X.L., Yan G.R.;
RT "An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and
RT tumorigenesis.";
RL Nat. Commun. 11:1685-1685(2020).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-99, AND SUBUNIT.
RX PubMed=20219472; DOI=10.1016/j.jmb.2010.02.043;
RA Benoit R.M., Meisner N.C., Kallen J., Graff P., Hemmig R., Cebe R.,
RA Ostermeier C., Widmer H., Auer M.;
RT "The X-ray crystal structure of the first RNA recognition motif and site-
RT directed mutagenesis suggest a possible HuR redox sensing mechanism.";
RL J. Mol. Biol. 397:1231-1244(2010).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-186 OF APOPROTEIN AND IN
RP COMPLEX WITH RNA, FUNCTION, RNA-BINDING, AND DOMAIN.
RX PubMed=23519412; DOI=10.1107/s0907444912047828;
RA Wang H., Zeng F., Liu Q., Liu H., Liu Z., Niu L., Teng M., Li X.;
RT "The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes
RT conformational changes during RNA binding.";
RL Acta Crystallogr. D 69:373-380(2013).
CC -!- FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs
CC and increases their stability (PubMed:14517288, PubMed:18285462,
CC PubMed:31358969). Involved in embryonic stem cell (ESC)
CC differentiation: preferentially binds mRNAs that are not methylated by
CC N6-methyladenosine (m6A), stabilizing them, promoting ESC
CC differentiation (By similarity). Has also been shown to be capable of
CC binding to m6A-containing mRNAs and contributes to MYC stability by
CC binding to m6A-containing MYC mRNAs (PubMed:32245947). Binds to poly-U
CC elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs
CC (PubMed:8626503, PubMed:17632515, PubMed:18285462, PubMed:23519412,
CC PubMed:14731398). Binds avidly to the AU-rich element in FOS and
CC IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds
CC to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and
CC AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in
CC vitro (PubMed:8626503). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA
CC to control their nuclear export induced by CDKN2A. Hence, may regulate
CC p53/TP53 expression and mediate in part the CDKN2A anti-proliferative
CC activity. May also bind with ZNF385A the CCNB1 mRNA (By similarity).
CC Increases the stability of the leptin mRNA harboring an AU-rich element
CC (ARE) in its 3' UTR (PubMed:29180010). {ECO:0000250|UniProtKB:P70372,
CC ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:14731398,
CC ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:23519412,
CC ECO:0000269|PubMed:29180010, ECO:0000269|PubMed:31358969,
CC ECO:0000269|PubMed:8626503}.
CC -!- SUBUNIT: Monomer and homodimer (in vitro) (PubMed:17632515,
CC PubMed:20219472). Interacts with ANP32A (PubMed:11729309). Interacts
CC with ZNF385A; the interaction is indirect and mRNA-dependent and may
CC regulate p53/TP53 expression (By similarity). Identified in a mRNP
CC complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1,
CC ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1
CC (PubMed:19029303). Interacts with AGO1 and AGO2 (PubMed:17932509).
CC Interacts with IGF2BP1; the interaction is enhanced by SEPIN14P20
CC peptide RBPR (PubMed:32245947, PubMed:29476152). Interacts with IGF2BP2
CC and IGF2BP3 (PubMed:23640942, PubMed:29476152). Interacts with HNRNPL
CC (PubMed:18161049). Interacts with DHX36; this interaction occurs in a
CC RNA-dependent manner (PubMed:14731398). Interacts with ILF3; this
CC interaction occurs in a RNA-dependent manner (PubMed:14731398).
CC Interacts with PLEKHN1 (PubMed:18191643, PubMed:27616329). Interacts
CC with SHFL; the interaction increases in presence of RNA
CC (PubMed:27974568). Interacts with YBX1; interaction recruits ELAVL1 on
CC C5-methylcytosine (m5C)-containing mRNAs, thereby promoting mRNA
CC stability (PubMed:31358969). {ECO:0000250|UniProtKB:P70372,
CC ECO:0000269|PubMed:11729309, ECO:0000269|PubMed:14731398,
CC ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:17932509,
CC ECO:0000269|PubMed:18161049, ECO:0000269|PubMed:18191643,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20219472,
CC ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:27616329,
CC ECO:0000269|PubMed:27974568, ECO:0000269|PubMed:32245947}.
CC -!- INTERACTION:
CC Q15717; P54253: ATXN1; NbExp=7; IntAct=EBI-374260, EBI-930964;
CC Q15717; O00560: SDCBP; NbExp=3; IntAct=EBI-374260, EBI-727004;
CC Q15717; Q13148: TARDBP; NbExp=7; IntAct=EBI-374260, EBI-372899;
CC Q15717; P0CG48: UBC; NbExp=4; IntAct=EBI-374260, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14517288,
CC ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462,
CC ECO:0000269|PubMed:19029303}. Nucleus {ECO:0000269|PubMed:14517288,
CC ECO:0000269|PubMed:17632515, ECO:0000269|PubMed:18285462}. Cytoplasm,
CC Stress granule {ECO:0000250|UniProtKB:P70372}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:29476152}. Note=Translocates into the cytoplasm
CC following phosphorylation by MAPKAPK2 (PubMed:14517288). Likewise,
CC phosphorylation by PRKCD promotes translocation from the nucleus into
CC the cytoplasm, where it is associated with free and cytoskeleton-bound
CC polysomes (PubMed:18285462).Localizes to the stress granules in the
CC presence of PLEKHN1 (By similarity). {ECO:0000250|UniProtKB:P70372,
CC ECO:0000269|PubMed:14517288, ECO:0000269|PubMed:18285462}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15717-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15717-2; Sequence=VSP_056148;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, liver, thymus and
CC muscle. {ECO:0000269|PubMed:8626503}.
CC -!- DOMAIN: The first RRM (RNA recognition motif) domain is essential for
CC binding to AU-rich elements. {ECO:0000269|PubMed:23519412}.
CC -!- PTM: Phosphorylated by MAPKAPK2 (PubMed:14517288). Phosphorylated by
CC PRKCD (PubMed:18285462). {ECO:0000269|PubMed:14517288,
CC ECO:0000269|PubMed:18285462}.
CC -!- PTM: Methylated at Arg-217 by CARM1 in macrophages in response to LPS
CC challenge. {ECO:0000269|PubMed:12237300}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ELAVL1ID44237ch19p13.html";
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DR EMBL; U38175; AAB41913.1; -; mRNA.
DR EMBL; BT009793; AAP88795.1; -; mRNA.
DR EMBL; AK301013; BAG62630.1; -; mRNA.
DR EMBL; AC008975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW68949.1; -; Genomic_DNA.
DR EMBL; BC003376; AAH03376.1; -; mRNA.
DR CCDS; CCDS12193.1; -. [Q15717-1]
DR RefSeq; NP_001410.2; NM_001419.2. [Q15717-1]
DR PDB; 3HI9; X-ray; 2.00 A; A/B/C/D=18-99.
DR PDB; 4ED5; X-ray; 2.00 A; A/B=18-186.
DR PDB; 4EGL; X-ray; 2.90 A; A=18-186.
DR PDB; 4FXV; X-ray; 1.90 A; A/B/C/D=20-99.
DR PDB; 5SZW; NMR; -; A=1-99.
DR PDB; 6G2K; X-ray; 2.01 A; A/B/C=243-326.
DR PDB; 6GC5; X-ray; 1.90 A; A/B/C/D=241-326.
DR PDB; 6GD1; X-ray; 2.01 A; A/B=243-326.
DR PDB; 6GD2; X-ray; 1.90 A; A/B/C=243-326.
DR PDB; 6GD3; X-ray; 1.35 A; A/B/C=243-326.
DR PDBsum; 3HI9; -.
DR PDBsum; 4ED5; -.
DR PDBsum; 4EGL; -.
DR PDBsum; 4FXV; -.
DR PDBsum; 5SZW; -.
DR PDBsum; 6G2K; -.
DR PDBsum; 6GC5; -.
DR PDBsum; 6GD1; -.
DR PDBsum; 6GD2; -.
DR PDBsum; 6GD3; -.
DR AlphaFoldDB; Q15717; -.
DR SMR; Q15717; -.
DR BioGRID; 108309; 1963.
DR CORUM; Q15717; -.
DR DIP; DIP-31291N; -.
DR IntAct; Q15717; 85.
DR MINT; Q15717; -.
DR STRING; 9606.ENSP00000385269; -.
DR BindingDB; Q15717; -.
DR ChEMBL; CHEMBL1250379; -.
DR GlyGen; Q15717; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15717; -.
DR MetOSite; Q15717; -.
DR PhosphoSitePlus; Q15717; -.
DR SwissPalm; Q15717; -.
DR BioMuta; ELAVL1; -.
DR DMDM; 20981691; -.
DR CPTAC; CPTAC-923; -.
DR EPD; Q15717; -.
DR jPOST; Q15717; -.
DR MassIVE; Q15717; -.
DR MaxQB; Q15717; -.
DR PaxDb; Q15717; -.
DR PeptideAtlas; Q15717; -.
DR PRIDE; Q15717; -.
DR ProteomicsDB; 60716; -. [Q15717-1]
DR Antibodypedia; 3933; 493 antibodies from 37 providers.
DR DNASU; 1994; -.
DR Ensembl; ENST00000407627.7; ENSP00000385269.1; ENSG00000066044.15. [Q15717-1]
DR Ensembl; ENST00000596459.5; ENSP00000472197.1; ENSG00000066044.15. [Q15717-1]
DR GeneID; 1994; -.
DR KEGG; hsa:1994; -.
DR MANE-Select; ENST00000407627.7; ENSP00000385269.1; NM_001419.3; NP_001410.2.
DR UCSC; uc002mjb.4; human. [Q15717-1]
DR CTD; 1994; -.
DR DisGeNET; 1994; -.
DR GeneCards; ELAVL1; -.
DR HGNC; HGNC:3312; ELAVL1.
DR HPA; ENSG00000066044; Low tissue specificity.
DR MIM; 603466; gene.
DR neXtProt; NX_Q15717; -.
DR OpenTargets; ENSG00000066044; -.
DR PharmGKB; PA27740; -.
DR VEuPathDB; HostDB:ENSG00000066044; -.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000155528; -.
DR HOGENOM; CLU_026186_2_2_1; -.
DR InParanoid; Q15717; -.
DR OMA; WQKHVTS; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; Q15717; -.
DR TreeFam; TF313377; -.
DR PathwayCommons; Q15717; -.
DR Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q15717; -.
DR SIGNOR; Q15717; -.
DR BioGRID-ORCS; 1994; 158 hits in 1086 CRISPR screens.
DR ChiTaRS; ELAVL1; human.
DR EvolutionaryTrace; Q15717; -.
DR GeneWiki; ELAVL1; -.
DR GenomeRNAi; 1994; -.
DR Pharos; Q15717; Tchem.
DR PRO; PR:Q15717; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15717; protein.
DR Bgee; ENSG00000066044; Expressed in endothelial cell and 207 other tissues.
DR ExpressionAtlas; Q15717; baseline and differential.
DR Genevisible; Q15717; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd12650; RRM1_Hu; 1.
DR DisProt; DP02564; -.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006548; ELAD_HU_SF.
DR InterPro; IPR034775; ELAV/Hu_RRM1.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..326
FT /note="ELAV-like protein 1"
FT /id="PRO_0000081577"
FT DOMAIN 20..98
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 106..186
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 244..322
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:18285462"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70372"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:12237300"
FT MOD_RES 217
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:18285462"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:18285462"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MGSGGRSAQVSTGQRAWLLPCRFLKNTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056148"
FT MUTAGEN 158
FT /note="S->A: Decreases phosphorylation by PRKCD."
FT /evidence="ECO:0000269|PubMed:18285462"
FT MUTAGEN 221
FT /note="S->A: Decreases phosphorylation by PRKCD. Nearly
FT abolishes phosphorylation by PRKCD and translocation from
FT the nucleus into the cytoplasm; when associated with A-
FT 318."
FT /evidence="ECO:0000269|PubMed:18285462"
FT MUTAGEN 318
FT /note="S->A: Decreases phosphorylation by PRKCD. Nearly
FT abolishes phosphorylation by PRKCD and translocation from
FT the nucleus into the cytoplasm; when associated with A-
FT 221."
FT /evidence="ECO:0000269|PubMed:18285462"
FT CONFLICT 180
FT /note="T -> A (in Ref. 1; AAB41913)"
FT /evidence="ECO:0000305"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:5SZW"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4FXV"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:4FXV"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:4FXV"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4FXV"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:4FXV"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4FXV"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4FXV"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4ED5"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4ED5"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:4ED5"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4ED5"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:4ED5"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4ED5"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:4ED5"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:4ED5"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:4ED5"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6GD3"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:6GD3"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6GD3"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:6GD3"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6GD3"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:6GD3"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:6GD3"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6GD3"
SQ SEQUENCE 326 AA; 36092 MW; 0B86143805264DEF CRC64;
MSNGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGHS
LGYGFVNYVT AKDAERAINT LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK
DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFNGH KPPGSSEPIT
VKFAANPNQN KNVALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG LSGVNVPGNA
SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
AIASLNGYRL GDKILQVSFK TNKSHK
